Development of Bacteriocinogenic Strains of Saccharomyces cerevisiae Heterologously Expressing and Secreting the Leaderless Enterocin L50 Peptides L50A and L50B from Enterococcus faecium L50

A segregationally stable expression and secretion vector for Saccharomyces cerevisiae, named pYABD01, was constructed by cloning the yeast gene region encoding the mating pheromone α-factor 1 secretion signal (MFα1s) into the S. cerevisiae high-copy-number expression vector pYES2. The structural gen...

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Bibliographic Details
Published in:Applied and Environmental Microbiology 2009-04, Vol.75 (8), p.2382-2392
Main Authors: Basanta, Antonio, Herranz, Carmen, Gutiérrez, Jorge, Criado, Raquel, Hernández, Pablo E, Cintas, Luis M
Format: Article
Language:English
Subjects:
Anti-Infective Agents - metabolism
Anti-Infective Agents - pharmacology
Antimicrobial peptides
Bacteria
Bacterial proteins
Bacteriocins - biosynthesis
Bacteriocins - genetics
Bacteriocins - pharmacology
Biological and medical sciences
Biotechnology
Cloning
Enterococcus faecium - genetics
Fundamental and applied biological sciences. Psychology
Gene expression
Mass Spectrometry
Microbial Sensitivity Tests
Microbiology
Peptides
Plasmids
Promoter Regions, Genetic
Protein Sorting Signals
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Yeast
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Summary:A segregationally stable expression and secretion vector for Saccharomyces cerevisiae, named pYABD01, was constructed by cloning the yeast gene region encoding the mating pheromone α-factor 1 secretion signal (MFα1s) into the S. cerevisiae high-copy-number expression vector pYES2. The structural genes of the two leaderless peptides of enterocin L50 (EntL50A and EntL50B) from Enterococcus faecium L50 were cloned, separately (entL50A or entL50B) and together (entL50AB), into pYABD01 under the control of the galactose-inducible promoter PGAL₁. The generation of recombinant S. cerevisiae strains heterologously expressing and secreting biologically active EntL50A and EntL50B demonstrates the suitability of the MFα1s-containing vector pYABD01 to direct processing and secretion of these antimicrobial peptides through the S. cerevisiae Sec system.
ISSN:0099-2240
1098-5336
1098-6596
DOI:10.1128/AEM.01476-08